메뉴 건너뛰기




Volumn 50, Issue 4-5, 2013, Pages 91-102

Characterization of immunoglobulin by mass spectrometry with applications for the clinical laboratory

Author keywords

Antibody; Autoimmunity; Biomarkers; Immunoglobulin; Mass spectrometry; Monoclonal therapeutics; Proteomics

Indexed keywords

AUTOANTIBODY; BIOLOGICAL MARKER; IMMUNOGLOBULIN; IMMUNOGLOBULIN A; IMMUNOGLOBULIN ANTIBODY; IMMUNOGLOBULIN G ANTIBODY; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; MONOCLONAL ANTIBODY; NICOTINIC RECEPTOR ANTIBODY; POLYCLONAL ANTIBODY; TUMOR ANTIGEN; UNCLASSIFIED DRUG;

EID: 84886773096     PISSN: 10408363     EISSN: 1549781X     Source Type: Journal    
DOI: 10.3109/10408363.2013.838206     Document Type: Review
Times cited : (15)

References (114)
  • 1
    • 0027372064 scopus 로고
    • Mechanism and regulation of immunoglobulin isotype switching
    • Coffman RL, Lebman DA, Rothman P. Mechanism and regulation of immunoglobulin isotype switching. Adv Immunol 1993;54: 229-70. (Pubitemid 23289254)
    • (1993) Advances in Immunology , vol.54 , pp. 229-270
    • Coffman, R.L.1    Lebman, D.A.2    Rothman, P.3
  • 2
    • 84855940327 scopus 로고    scopus 로고
    • Autoantibody diagnostics in clinical practice
    • Conrad K, Roggenbuck D, Reinhold D, et al. Autoantibody diagnostics in clinical practice. Autoimmun Rev 2012;11:207-11.
    • (2012) Autoimmun Rev , vol.11 , pp. 207-211
    • Conrad, K.1    Roggenbuck, D.2    Reinhold, D.3
  • 3
    • 77951067848 scopus 로고    scopus 로고
    • Autoantibodies to tumor-associated antigens as cancer biomarkers
    • Belousov PV, Kuprash DV, Nedospasov SA, et al. Autoantibodies to tumor-associated antigens as cancer biomarkers. Curr Mol Med 2010;10:115-22.
    • (2010) Curr Mol Med , vol.10 , pp. 115-122
    • Belousov, P.V.1    Kuprash, D.V.2    Nedospasov, S.A.3
  • 4
    • 34848906018 scopus 로고    scopus 로고
    • The four most common pediatric immunodeficiencies
    • Stiehm RE. The four most common pediatric immunodeficiencies. Adv Exp Med Biol 2007;601:15-26.
    • (2007) Adv Exp Med Biol , vol.601 , pp. 15-26
    • Stiehm, R.E.1
  • 5
    • 0036301546 scopus 로고    scopus 로고
    • Are there any clinical indications for measuring IgG subclasses?
    • DOI 10.1258/000456302760042678
    • Maguire GA, Kumararatne DS, Joyce HJ. Are there any clinical indications for measuring IgG subclasses? Ann Clin Biochem 2002;39:374-7. (Pubitemid 34743639)
    • (2002) Annals of Clinical Biochemistry , vol.39 , Issue.4 , pp. 374-377
    • Maguire, G.A.1    Kumararatne, D.S.2    Joyce, H.J.3
  • 7
    • 84886800660 scopus 로고    scopus 로고
    • Challenges and controversies in anti-nuclear antibody testing
    • Rollins G. Challenges and controversies in anti-nuclear antibody testing. Clin Lab News 2009;34:15.
    • (2009) Clin Lab News , vol.34 , pp. 15
    • Rollins, G.1
  • 8
  • 9
    • 78650787263 scopus 로고    scopus 로고
    • Pattern on the antinuclear antibody-HEp-2 test is a critical parameter for discriminating antinuclear antibody-positive healthy individuals and patients with autoimmune rheumatic diseases
    • Mariz HA, Sato EI, Barbosa SH, et al. Pattern on the antinuclear antibody-HEp-2 test is a critical parameter for discriminating antinuclear antibody-positive healthy individuals and patients with autoimmune rheumatic diseases. Arthrit Rheumat 2011;63: 191-200.
    • (2011) Arthrit Rheumat , vol.63 , pp. 191-200
    • Mariz, H.A.1    Sato, E.I.2    Barbosa, S.H.3
  • 10
    • 28744449120 scopus 로고    scopus 로고
    • From ANA to ENA: How to proceed?
    • DOI 10.1016/j.autrev.2005.05.007, PII S1568997205000819
    • Damoiseaux JGMC, Cohen Tervaert JW. From ANA to ENA: how to proceed? Autoimmun Rev 2006;5:10-17. (Pubitemid 41759437)
    • (2006) Autoimmunity Reviews , vol.5 , Issue.1 , pp. 10-17
    • Damoiseaux, J.G.M.C.1    Cohen Tervaert, J.W.2
  • 11
    • 34848899292 scopus 로고    scopus 로고
    • Evaluation of the BioPlex 2200 ANA screen for the detection of antinuclear antibodies and comparison with conventional methods
    • DOI 10.1196/annals.1398.030, Autoimmunity, Part A Basic Principles and New Diagnostic Tools
    • Desplat-Jego S, Bardin N, Larida B, et al. Evaluation of the BioPlex 2200 ANA screen for the detection of antinuclear antibodies and comparison with conventional methods. Ann N Y Acad Sci 2007;1109:245-55. (Pubitemid 47511367)
    • (2007) Annals of the New York Academy of Sciences , vol.1109 , pp. 245-255
    • Desplat-Jego, S.1    Bardin, N.2    Larida, B.3    Sanmarco, M.4
  • 12
    • 60549107323 scopus 로고    scopus 로고
    • Case records of the Massachusetts General Hospital. Case 5-2009. A 47-year-old woman with a rash and numbness and pain in the legs
    • Kroshinsky D, Stone JH, Bloch DB, et al. Case records of the Massachusetts General Hospital. Case 5-2009. A 47-year-old woman with a rash and numbness and pain in the legs. New Engl J Med 2009;360:711-20.
    • (2009) New Engl J Med , vol.360 , pp. 711-720
    • Kroshinsky, D.1    Stone, J.H.2    Bloch, D.B.3
  • 14
    • 84872503060 scopus 로고    scopus 로고
    • Characterization of therapeutic antibodies and related products
    • Beck A, Wagner-Rousset E, Ayoub D, et al. Characterization of therapeutic antibodies and related products. Anal Chem 2013;85: 715-36.
    • (2013) Anal Chem , vol.85 , pp. 715-736
    • Beck, A.1    Wagner-Rousset, E.2    Ayoub, D.3
  • 15
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, et al. Electrospray ionization for mass spectrometry of large biomolecules. Science 1989;246: 64-71. (Pubitemid 19252085)
    • (1989) Science , vol.246 , Issue.4926 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 16
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10 000 daltons
    • Karas M, Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10 000 daltons. Anal Chem 1988;60:2299-301.
    • (1988) Anal Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 17
    • 84855200643 scopus 로고    scopus 로고
    • Principles of electrospray ionization
    • 009407
    • Wilm M. Principles of electrospray ionization. Mol Cell Prot MCP 2011;10:M111 009407.
    • (2011) Mol Cell Prot MCP , vol.10
    • Wilm, M.1
  • 18
    • 79959458959 scopus 로고    scopus 로고
    • The application of MALDI TOF MS in biopharmaceutical research
    • Kafka AP, Kleffmann T, Rades T, et al. The application of MALDI TOF MS in biopharmaceutical research. Int J Pharmaceut 2011;417:70-82.
    • (2011) Int J Pharmaceut , vol.417 , pp. 70-82
    • Kafka, A.P.1    Kleffmann, T.2    Rades, T.3
  • 19
    • 59149092065 scopus 로고    scopus 로고
    • Mass spectrometry for structural characterization of therapeutic antibodies
    • Zhang Z, Pan H, Chen X. Mass spectrometry for structural characterization of therapeutic antibodies. Mass Spectrometr Rev 2009;28:147-76.
    • (2009) Mass Spectrometr Rev , vol.28 , pp. 147-176
    • Zhang, Z.1    Pan, H.2    Chen, X.3
  • 20
    • 0027332396 scopus 로고
    • Kappa marker typing with high-performance liquid chromatography: Identification of kappa marker specific tryptic peptide from the kappa light chain of immunoglobulin G
    • Iida R, Yasuda T, Nadano D, et al. Kappa marker typing with high-performance liquid chromatography: identification of kappa marker specific tryptic peptide from the kappa light chain of immunoglobulin G. J Chromatogr 1993;622:9-12.
    • (1993) J Chromatogr , vol.622 , pp. 9-12
    • Iida, R.1    Yasuda, T.2    Nadano, D.3
  • 21
    • 84860408352 scopus 로고    scopus 로고
    • Comparison of two-dimensional gel electrophoresis patterns and MALDI-TOF MS analysis of therapeutic recombinant monoclonal antibodies trastuzumab and rituximab
    • Nebija D, Kopelent-Frank H, Urban E, et al. Comparison of two-dimensional gel electrophoresis patterns and MALDI-TOF MS analysis of therapeutic recombinant monoclonal antibodies trastuzumab and rituximab. J Pharmaceut Biomed Anal 2011; 56:684-91.
    • (2011) J Pharmaceut Biomed Anal , vol.56 , pp. 684-691
    • Nebija, D.1    Kopelent-Frank, H.2    Urban, E.3
  • 23
    • 84870656120 scopus 로고    scopus 로고
    • Assessment of stable isotope incorporation into recombinant proteins
    • Zhang X, Luo Q, Apostol I, et al. Assessment of stable isotope incorporation into recombinant proteins. Anal Biochem 2013;433: 137-49.
    • (2013) Anal Biochem , vol.433 , pp. 137-149
    • Zhang, X.1    Luo, Q.2    Apostol, I.3
  • 25
    • 4444301306 scopus 로고    scopus 로고
    • Absolute quantification of the model biomarker prostate-specific antigen in serum by LC-MS/MS using protein cleavage and isotope dilution mass spectrometry
    • DOI 10.1021/pr049963d
    • Barnidge DR, Goodmanson MK, Klee GG, et al. Absolute quantification of the model biomarker prostate-specific antigen in serum by LC-MS/MS using protein cleavage and isotope dilution mass spectrometry. J Prot Res 2004;3:644-52. (Pubitemid 39207371)
    • (2004) Journal of Proteome Research , vol.3 , Issue.3 , pp. 644-652
    • Barnidge, D.R.1    Goodmanson, M.K.2    Klee, G.G.3    Muddiman, D.C.4
  • 26
    • 44949213072 scopus 로고    scopus 로고
    • Towards absolute quantification of therapeutic monoclonal antibody in serum by LC-MS/MS using isotope-labeled antibody standard and protein cleavage isotope dilution mass spectrometry
    • DOI 10.1021/ac800205s
    • Heudi O, Barteau S, Zimmer D, et al. Towards absolute quantification of therapeutic monoclonal antibody in serum by LC-MS/MS using isotope-labeled antibody standard and protein cleavage isotope dilution mass spectrometry. Anal Chem 2008;80: 4200-7. (Pubitemid 351812775)
    • (2008) Analytical Chemistry , vol.80 , Issue.11 , pp. 4200-4207
    • Heudi, O.1    Barteau, S.2    Zimmer, D.3    Schmidt, J.4    Bill, K.5    Lehmann, N.6    Bauer, C.7    Kretz, O.8
  • 27
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, Yates Iii JR. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrometry 1994;5:976-89.
    • (1994) J Am Soc Mass Spectrometry , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 28
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, et al. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999;20:3551-67. (Pubitemid 30007252)
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 29
    • 33750979860 scopus 로고    scopus 로고
    • General framework for developing and evaluating database scoring algorithms using the TANDEM search engine
    • DOI 10.1093/bioinformatics/btl379
    • MacLean B, Eng JK, Beavis RC, et al. General framework for developing and evaluating database scoring algorithms using the TANDEM search engine. Bioinformatics 2006;22:2830-2. (Pubitemid 44742409)
    • (2006) Bioinformatics , vol.22 , Issue.22 , pp. 2830-2832
    • MacLean, B.1    Eng, J.K.2    Beavis, R.C.3    McIntosh, M.4
  • 31
    • 77953155288 scopus 로고    scopus 로고
    • Template proteoge-nomics: Sequencing whole proteins using an imperfect database
    • Castellana NE, Pham V, Arnott D, et al. Template proteoge-nomics: sequencing whole proteins using an imperfect database. Mol Cell Prot 2010;9:1260-70.
    • (2010) Mol Cell Prot , vol.9 , pp. 1260-1270
    • Castellana, N.E.1    Pham, V.2    Arnott, D.3
  • 32
    • 84860567341 scopus 로고    scopus 로고
    • Characterization of the isomerization products of aspartate residues at two different sites in a monoclonal antibody
    • Sreedhara A, Cordoba A, Zhu Q, et al. Characterization of the isomerization products of aspartate residues at two different sites in a monoclonal antibody. Pharmaceut Res 2012;29:187-97.
    • (2012) Pharmaceut Res , vol.29 , pp. 187-197
    • Sreedhara, A.1    Cordoba, A.2    Zhu, Q.3
  • 33
    • 68949107399 scopus 로고    scopus 로고
    • Characterization of the photodegradation of a human IgG1 monoclonal antibody formulated as a high-concentration liquid dosage form
    • Qi P, Volkin DB, Zhao H, et al. Characterization of the photodegradation of a human IgG1 monoclonal antibody formulated as a high-concentration liquid dosage form. J Pharmaceut Sci 2009;98:3117-30.
    • (2009) J Pharmaceut Sci , vol.98 , pp. 3117-3130
    • Qi, P.1    Volkin, D.B.2    Zhao, H.3
  • 34
    • 79953316060 scopus 로고    scopus 로고
    • HIC resolution of an IgG1 with an oxidized Trp in a complementarity determining region
    • Boyd D, Kaschak T, Yan B. HIC resolution of an IgG1 with an oxidized Trp in a complementarity determining region. J Chromatogr B, Anal Technol Biomed Life Sci 2011;879:955-60.
    • (2011) J Chromatogr B, Anal Technol Biomed Life Sci , vol.879 , pp. 955-960
    • Boyd, D.1    Kaschak, T.2    Yan, B.3
  • 35
    • 60849113728 scopus 로고    scopus 로고
    • Trends in glycosylation, glycoanalysis and glycoengineering of therapeutic antibodies and Fc-fusion proteins
    • Beck A, Wagner-Rousset E, Bussat MC, et al. Trends in glycosylation, glycoanalysis and glycoengineering of therapeutic antibodies and Fc-fusion proteins. Curr Pharmaceut Biotechnol 2008;9:482-501.
    • (2008) Curr Pharmaceut Biotechnol , vol.9 , pp. 482-501
    • Beck, A.1    Wagner-Rousset, E.2    Bussat, M.C.3
  • 36
    • 67649394336 scopus 로고    scopus 로고
    • Recombinant antibody therapeutics: The impact of glycosylation on mechanisms of action
    • Jefferis R. Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action. Trends Pharmacol Sci 2009;30:356-62.
    • (2009) Trends Pharmacol Sci , vol.30 , pp. 356-362
    • Jefferis, R.1
  • 37
    • 28844463354 scopus 로고    scopus 로고
    • Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro
    • DOI 10.1021/bp050228w
    • Hodoniczky J, Zheng YZ, James DC. Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro. Biotechnol Progr 2005;21:1644-52. (Pubitemid 41778987)
    • (2005) Biotechnology Progress , vol.21 , Issue.6 , pp. 1644-1652
    • Hodoniczky, J.1    Yuan, Z.Z.2    James, D.C.3
  • 39
    • 77956931053 scopus 로고    scopus 로고
    • A systematic approach to protein glycosylation analysis: A path through the maze
    • Marino K, Bones J, Kattla JJ, et al. A systematic approach to protein glycosylation analysis: a path through the maze. Nature Chem Biol 2010;6:713-23.
    • (2010) Nature Chem Biol , vol.6 , pp. 713-723
    • Marino, K.1    Bones, J.2    Kattla, J.J.3
  • 40
    • 79551499066 scopus 로고    scopus 로고
    • Glycan analysis by modern instrumental methods
    • Pabst M, Altmann F. Glycan analysis by modern instrumental methods. Proteomics 2011;11:631-43.
    • (2011) Proteomics , vol.11 , pp. 631-643
    • Pabst, M.1    Altmann, F.2
  • 41
    • 84868553080 scopus 로고    scopus 로고
    • High-throughput work flow for IgG Fc-glycosylation analysis of biotechnological samples
    • Reusch D, Haberger M, Selman MH, et al. High-throughput work flow for IgG Fc-glycosylation analysis of biotechnological samples. Anal Biochem 2013;432:82-9.
    • (2013) Anal Biochem , vol.432 , pp. 82-89
    • Reusch, D.1    Haberger, M.2    Selman, M.H.3
  • 42
    • 0034652301 scopus 로고    scopus 로고
    • Automated identification of amino acid sequence variations in proteins by HPLC/microspray tandem mass spectrometry
    • DOI 10.1021/ac991025n
    • Gatlin CL, Eng JK, Cross ST, et al. Automated identification of amino acid sequence variations in proteins by HPLC/microspray tandem mass spectrometry. Anal Chem 2000;72:757-63. (Pubitemid 30111516)
    • (2000) Analytical Chemistry , vol.72 , Issue.4 , pp. 757-763
    • Gatlin, C.L.1    Eng, J.K.2    Cross, S.T.3    Detter, J.C.4    Yates III, J.R.5
  • 43
    • 77953677787 scopus 로고    scopus 로고
    • Detecting low level sequence variants in recombinant monoclonal antibodies
    • Yang Y, Strahan A, Li C, et al. Detecting low level sequence variants in recombinant monoclonal antibodies. MAbs 2010;2:285-98.
    • (2010) MAbs , vol.2 , pp. 285-298
    • Yang, Y.1    Strahan, A.2    Li, C.3
  • 44
    • 79251500018 scopus 로고    scopus 로고
    • Resurrection of a clinical antibody: Template proteogenomic de novo proteomic sequencing and reverse engineering of an anti-lymphotoxin-A antibody
    • Castellana NE, McCutcheon K, Pham VC, et al. Resurrection of a clinical antibody: template proteogenomic de novo proteomic sequencing and reverse engineering of an anti-lymphotoxin-a antibody. Proteomics 2011;11:395-405.
    • (2011) Proteomics , vol.11 , pp. 395-405
    • Castellana, N.E.1    McCutcheon, K.2    Pham, V.C.3
  • 45
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson L, Hunter CL. Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol Cell Proteomics 2006;5:573-88.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 46
    • 84861142055 scopus 로고    scopus 로고
    • High-throughput method development for sensitive, accurate, and reproducible quantification of therapeutic monoclonal antibodies in tissues using orthogonal array optimization and nano liquid chromatography/selected reaction monitoring mass spectrometry
    • Duan X, Abuqayyas L, Dai L, et al. High-throughput method development for sensitive, accurate, and reproducible quantification of therapeutic monoclonal antibodies in tissues using orthogonal array optimization and nano liquid chromatography/selected reaction monitoring mass spectrometry. Anal Chem 2012; 84:4373-82.
    • (2012) Anal Chem , vol.84 , pp. 4373-4382
    • Duan, X.1    Abuqayyas, L.2    Dai, L.3
  • 47
    • 84869033783 scopus 로고    scopus 로고
    • High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies
    • Rose RJ, Damoc E, Denisov E, et al. High-sensitivity Orbitrap mass analysis of intact macromolecular assemblies. Nat Methods 2012;9:1084-6.
    • (2012) Nat Methods , vol.9 , pp. 1084-1086
    • Rose, R.J.1    Damoc, E.2    Denisov, E.3
  • 48
    • 0025217244 scopus 로고
    • Primary sequence information from intact proteins by electrospray ionization tandem mass spectrometry
    • Loo JA, Edmonds CG, Smith RD. Primary sequence information from intact proteins by electrospray ionization tandem mass spectrometry. Science 1990;248:201-4.
    • (1990) Science , vol.248 , pp. 201-204
    • Loo, J.A.1    Edmonds, C.G.2    Smith, R.D.3
  • 49
    • 0025424768 scopus 로고
    • New developments in biochemical mass spectrometry: Electrospray ionization
    • Smith RD, Loo JA, Edmonds CG, et al. New developments in biochemical mass spectrometry: electrospray ionization. Anal Chem 1990;62:882-99.
    • (1990) Anal Chem , vol.62 , pp. 882-899
    • Smith, R.D.1    Loo, J.A.2    Edmonds, C.G.3
  • 50
    • 79952012529 scopus 로고    scopus 로고
    • The emerging process of Top Down mass spectrometry for protein analysis: Biomarkers, protein-therapeutics, and achieving high throughput
    • Kellie JF, Tran JC, Lee JE, et al. The emerging process of Top Down mass spectrometry for protein analysis: biomarkers, protein-therapeutics, and achieving high throughput. Mol Biosyst 2010;6:1532-9.
    • (2010) Mol Biosyst , vol.6 , pp. 1532-1539
    • Kellie, J.F.1    Tran, J.C.2    Lee, J.E.3
  • 52
    • 0028910758 scopus 로고
    • Mass spectrometry of the humanized monoclonal antibody CAMPATH 1H
    • Ashton DS, Beddell CR, Cooper DJ, et al. Mass spectrometry of the humanized monoclonal antibody CAMPATH 1H. Anal Chem 1995;67:835-42.
    • (1995) Anal Chem , vol.67 , pp. 835-842
    • Ashton, D.S.1    Beddell, C.R.2    Cooper, D.J.3
  • 53
    • 77957333488 scopus 로고    scopus 로고
    • Mass spectrometric analysis of intact human monoclonal antibody aggregates fractionated by size-exclusion chromatography
    • Kukrer B, Filipe V, van Duijn E, et al. Mass spectrometric analysis of intact human monoclonal antibody aggregates fractionated by size-exclusion chromatography. Pharm Res 2010;27:2197-204.
    • (2010) Pharm Res , vol.27 , pp. 2197-2204
    • Kukrer, B.1    Filipe, V.2    Van Duijn, E.3
  • 54
    • 80052512948 scopus 로고    scopus 로고
    • Species-specific determinants in the IgG CH3 domain enable Fab-arm exchange by affecting the noncovalent CH3-CH3 interaction strength
    • Labrijn AF, Rispens T, Meesters J, et al. Species-specific determinants in the IgG CH3 domain enable Fab-arm exchange by affecting the noncovalent CH3-CH3 interaction strength. J Immunol 2011;187:3238-46.
    • (2011) J Immunol , vol.187 , pp. 3238-3246
    • Labrijn, A.F.1    Rispens, T.2    Meesters, J.3
  • 55
    • 67650754060 scopus 로고    scopus 로고
    • Mass measurement and top-down HPLC/MS analysis of intact monoclonal antibodies on a hybrid linear quadrupole ion trap-Orbitrap mass spectrometer
    • Bondarenko PV, Second TP, Zabrouskov V, et al. Mass measurement and top-down HPLC/MS analysis of intact monoclonal antibodies on a hybrid linear quadrupole ion trap-Orbitrap mass spectrometer. J Am Soc Mass Spectrom 2009;20:1415-24.
    • (2009) J Am Soc Mass Spectrom , vol.20 , pp. 1415-1424
    • Bondarenko, P.V.1    Second, T.P.2    Zabrouskov, V.3
  • 56
    • 57849115243 scopus 로고    scopus 로고
    • High-throughput immunoglobulin G N-glycan characterization using rapid resolution reverse-phase chromatography tandem mass spectrometry
    • Prater BD, Connelly HM, Qin Q, et al. High-throughput immunoglobulin G N-glycan characterization using rapid resolution reverse-phase chromatography tandem mass spectrometry. Anal Biochem 2009;385:69-79.
    • (2009) Anal Biochem , vol.385 , pp. 69-79
    • Prater, B.D.1    Connelly, H.M.2    Qin, Q.3
  • 57
    • 65549096754 scopus 로고    scopus 로고
    • Discrimination among IgG1-kappa monoclonal antibodies produced by two cell lines using charge state distributions in nanoESI-TOF mass spectra
    • Zamani L, Lindholm J, Ilag LL, et al. Discrimination among IgG1-kappa monoclonal antibodies produced by two cell lines using charge state distributions in nanoESI-TOF mass spectra. J Am Soc Mass Spectrom 2009;20:1030-6.
    • (2009) J Am Soc Mass Spectrom , vol.20 , pp. 1030-1036
    • Zamani, L.1    Lindholm, J.2    Ilag, L.L.3
  • 58
    • 77953665930 scopus 로고    scopus 로고
    • Structural and functional characterization of the trifunctional antibody catumaxomab
    • Chelius D, Ruf P, Gruber P, et al. Structural and functional characterization of the trifunctional antibody catumaxomab. MAbs 2010;2:309-19.
    • (2010) MAbs , vol.2 , pp. 309-319
    • Chelius, D.1    Ruf, P.2    Gruber, P.3
  • 59
    • 81255211544 scopus 로고    scopus 로고
    • An innovative approach for the characterization of the isoforms of a monoclonal antibody product
    • Sundaram S, Matathia A, Qian J, et al. An innovative approach for the characterization of the isoforms of a monoclonal antibody product. MAbs 2011;3:505-12.
    • (2011) MAbs , vol.3 , pp. 505-512
    • Sundaram, S.1    Matathia, A.2    Qian, J.3
  • 60
    • 77956237886 scopus 로고    scopus 로고
    • Rapid whole monoclonal antibody analysis by mass spectrometry: An ultra scale-down study of the effect of harvesting by centrifugation on the post-translational modification profile
    • Reid CQ, Tait A, Baldascini H, et al. Rapid whole monoclonal antibody analysis by mass spectrometry: an ultra scale-down study of the effect of harvesting by centrifugation on the post-translational modification profile. Biotechnol Bioeng 2010;107: 85-95.
    • (2010) Biotechnol Bioeng , vol.107 , pp. 85-95
    • Reid, C.Q.1    Tait, A.2    Baldascini, H.3
  • 61
    • 82555170557 scopus 로고    scopus 로고
    • Structural analysis of intact monoclonal antibodies by electron transfer dissociation mass spectrometry
    • Tsybin YO, Fornelli L, Stoermer C, et al. Structural analysis of intact monoclonal antibodies by electron transfer dissociation mass spectrometry. Anal Chem 2011;83:8919-27.
    • (2011) Anal Chem , vol.83 , pp. 8919-8927
    • Tsybin, Y.O.1    Fornelli, L.2    Stoermer, C.3
  • 62
    • 56249117292 scopus 로고    scopus 로고
    • Top-down N-terminal sequencing of Immunoglobulin subunits with electrospray ioniza-tion time of flight mass spectrometry
    • Ren D, Pipes GD, Hambly D, et al. Top-down N-terminal sequencing of Immunoglobulin subunits with electrospray ioniza-tion time of flight mass spectrometry. Anal Biochem 2009;384: 42-8.
    • (2009) Anal Biochem , vol.384 , pp. 42-48
    • Ren, D.1    Pipes, G.D.2    Hambly, D.3
  • 63
    • 77951064458 scopus 로고    scopus 로고
    • Top-down de Novo protein sequencing of a 13.6 kDa camelid single heavy chain antibody by matrix-assisted laser desorption ionization-time-of-flight/ time-of-flight mass spectrometry
    • Resemann A, Wunderlich D, Rothbauer U, et al. Top-down de Novo protein sequencing of a 13.6 kDa camelid single heavy chain antibody by matrix-assisted laser desorption ionization-time-of-flight/time-of-flight mass spectrometry. Anal Chem 2010;82: 3283-92.
    • (2010) Anal Chem , vol.82 , pp. 3283-3292
    • Resemann, A.1    Wunderlich, D.2    Rothbauer, U.3
  • 64
    • 0242569357 scopus 로고    scopus 로고
    • "Top Down" Characterization Is a Complementary Technique to Peptide Sequencing for Identifying Protein Species in Complex Mixtures
    • DOI 10.1021/pr034008u
    • Nemeth-Cawley JF, Tangarone BS, Rouse JC. "Top Down" characterization is a complementary technique to peptide sequencing for identifying protein species in complex mixtures. J Proteome Res 2003;2:495-505. (Pubitemid 37376844)
    • (2003) Journal of Proteome Research , vol.2 , Issue.5 , pp. 495-505
    • Nemeth-Cawley, J.F.1    Tangarone, B.S.2    Rouse, J.C.3
  • 67
    • 33746273552 scopus 로고    scopus 로고
    • Identification of cysteinylation of a free cysteine in the Fab region of a recombinant monoclonal IgG1 antibody using Lys-C limited proteolysis coupled with LC/MS analysis
    • DOI 10.1016/j.ab.2006.05.037, PII S0003269706004064
    • Gadgil HS, Bondarenko PV, Pipes GD, et al. Identification of cysteinylation of a free cysteine in the Fab region of a recombinant monoclonal IgG1 antibody using Lys-C limited proteolysis coupled with LC/MS analysis. Anal Biochem 2006;355:165-74. (Pubitemid 44107324)
    • (2006) Analytical Biochemistry , vol.355 , Issue.2 , pp. 165-174
    • Gadgil, H.S.1    Bondarenko, P.V.2    Pipes, G.D.3    Dillon, T.M.4    Banks, D.5    Abel, J.6    Kleemann, G.R.7    Treuheit, M.J.8
  • 68
    • 39149138479 scopus 로고    scopus 로고
    • Proteolysis of purified IgGs by human and bacterial enzymes in vitro and the detection of specific proteolytic fragments of endogenous IgG in rheumatoid synovial fluid
    • Ryan MH, Petrone D, Nemeth JF, et al. Proteolysis of purified IgGs by human and bacterial enzymes in vitro and the detection of specific proteolytic fragments of endogenous IgG in rheumatoid synovial fluid. Mol Immunol 2008;45:1837-46.
    • (2008) Mol Immunol , vol.45 , pp. 1837-1846
    • Ryan, M.H.1    Petrone, D.2    Nemeth, J.F.3
  • 69
    • 78149353033 scopus 로고    scopus 로고
    • Middle-down fragmentation for the identification and quantitation of site-specific methionine oxidation in an IgG1 molecule
    • Pipes GD, Campbell P, Bondarenko PV, et al. Middle-down fragmentation for the identification and quantitation of site-specific methionine oxidation in an IgG1 molecule. J Pharm Sci 2010;99:4469-76.
    • (2010) J Pharm Sci , vol.99 , pp. 4469-4476
    • Pipes, G.D.1    Campbell, P.2    Bondarenko, P.V.3
  • 70
    • 75149170146 scopus 로고    scopus 로고
    • Structural characterization of intact antibodies by high-resolution LTQ Orbitrap mass spectrometry
    • Zhang J, Liu H, Katta V. Structural characterization of intact antibodies by high-resolution LTQ Orbitrap mass spectrometry. J Mass Spectrom 2010;45:112-20.
    • (2010) J Mass Spectrom , vol.45 , pp. 112-120
    • Zhang, J.1    Liu, H.2    Katta, V.3
  • 71
    • 82455171807 scopus 로고    scopus 로고
    • Rapid LC-MS screening for IgG Fc modifications and allelic variants in blood
    • Goetze AM, Zhang Z, Liu L, et al. Rapid LC-MS screening for IgG Fc modifications and allelic variants in blood. Mol Immunol 2011;49:338-52.
    • (2011) Mol Immunol , vol.49 , pp. 338-352
    • Goetze, A.M.1    Zhang, Z.2    Liu, L.3
  • 74
    • 0021285559 scopus 로고
    • Preferential utilization of the most J(H)-proximal V(H) gene segments in pre-B-cell lines
    • DOI 10.1038/311727a0
    • Yancopoulos GD, Desiderio SV, Paskind M, et al. Preferential utilization of the most JH-proximal VH gene segments in pre-B-cell lines. Nature 1984;311:727-33. (Pubitemid 14008986)
    • (1984) Nature , vol.311 , Issue.5988 , pp. 727-733
    • Yancopoulos, G.D.1    Desiderio, S.V.2    Paskind, M.3
  • 75
    • 0025921739 scopus 로고
    • VH gene usage in humans: Biased usage of the VH6 gene in immature B lymphoid cells
    • Berman JE, Nickerson KG, Pollock RR, et al. VH gene usage in humans: biased usage of the VH6 gene in immature B lymphoid cells. Eur J Immunol 1991;21:1311-4.
    • (1991) Eur J Immunol , vol.21 , pp. 1311-1314
    • Berman, J.E.1    Nickerson, K.G.2    Pollock, R.R.3
  • 76
    • 0026002998 scopus 로고
    • Diversity of immunoglobulin heavy chain gene segment rearrangement in B lymphoblastoid cell lines from X-linked agammaglobulinemia patients
    • Timmers E, Kenter M, Thompson A, et al. Diversity of immunoglobulin heavy chain gene segment rearrangement in B lymphoblastoid cell lines from X-linked agammaglobulinemia patients. Eur J Immunol 1991;21:2355-63.
    • (1991) Eur J Immunol , vol.21 , pp. 2355-2363
    • Timmers, E.1    Kenter, M.2    Thompson, A.3
  • 77
    • 79955109675 scopus 로고    scopus 로고
    • Determinism and stochasticity during maturation of the zebrafish antibody repertoire
    • Jiang N, Weinstein JA, Penland L, et al. Determinism and stochasticity during maturation of the zebrafish antibody repertoire. Proc Natl Acad Sci USA 2011;108:5348-53.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 5348-5353
    • Jiang, N.1    Weinstein, J.A.2    Penland, L.3
  • 78
    • 65649122270 scopus 로고    scopus 로고
    • High-throughput sequencing of the zebrafish antibody repertoire
    • Weinstein JA, Jiang N, White RA, et al. High-throughput sequencing of the zebrafish antibody repertoire. Science 2009; 324:807-10.
    • (2009) Science , vol.324 , pp. 807-810
    • Weinstein, J.A.1    Jiang, N.2    White, R.A.3
  • 79
    • 84874092680 scopus 로고    scopus 로고
    • Lineage structure of the human antibody repertoire in response to influenza vaccination
    • Jiang N, He J, Weinstein JA, et al. Lineage structure of the human antibody repertoire in response to influenza vaccination. Sci Transl Med 2013;5:171ra19.
    • (2013) Sci Transl Med , vol.5
    • Jiang, N.1    He, J.2    Weinstein, J.A.3
  • 80
    • 79953297689 scopus 로고    scopus 로고
    • Heavy-chain complementarity-determining regions determine conformation selectivity of anti-abeta antibodies
    • Sehlin D, Hedlund M, Lord A, et al. Heavy-chain complementarity- determining regions determine conformation selectivity of anti-abeta antibodies. Neurodegener Dis 2011;8:117-23.
    • (2011) Neurodegener Dis , vol.8 , pp. 117-123
    • Sehlin, D.1    Hedlund, M.2    Lord, A.3
  • 81
    • 77956555909 scopus 로고    scopus 로고
    • Immune responses are characterized by specific shared immunoglobulin peptides that can be detected by proteomic techniques
    • VanDuijn MM, Dekker LJ, Zeneyedpour L, et al. Immune responses are characterized by specific shared immunoglobulin peptides that can be detected by proteomic techniques. J Biol Chem 2010;285:29247-53.
    • (2010) J Biol Chem , vol.285 , pp. 29247-29253
    • Vanduijn, M.M.1    Dekker, L.J.2    Zeneyedpour, L.3
  • 82
    • 77954581170 scopus 로고    scopus 로고
    • Sequencing and quantifying IgG fragments and antigen-binding regions by mass spectrometry
    • de Costa D, Broodman I, Vanduijn MM, et al. Sequencing and quantifying IgG fragments and antigen-binding regions by mass spectrometry. J Proteome Res 2010;9:2937-45.
    • (2010) J Proteome Res , vol.9 , pp. 2937-2945
    • De Costa, D.1    Broodman, I.2    Vanduijn, M.M.3
  • 83
    • 79251637745 scopus 로고    scopus 로고
    • An antibody-based biomarker discovery method by mass spectrometry sequencing of complementarity determining regions
    • Dekker LJ, Zeneyedpour L, Brouwer E, et al. An antibody-based biomarker discovery method by mass spectrometry sequencing of complementarity determining regions. Anal Bioanal Chem 2011; 399:1081-91.
    • (2011) Anal Bioanal Chem , vol.399 , pp. 1081-1091
    • Dekker, L.J.1    Zeneyedpour, L.2    Brouwer, E.3
  • 84
    • 84886775454 scopus 로고    scopus 로고
    • Monitoring plasma cell specific heavy chain variable region tryptic peptides in patients with multiple myeloma using LC-MS/MS
    • submitted for publication
    • Barnidge DR, Graham RP, Theis JD, et al. Monitoring plasma cell specific heavy chain variable region tryptic peptides in patients with multiple myeloma using LC-MS/MS. Data submitted for publication.
    • Data
    • Barnidge, D.R.1    Graham, R.P.2    Theis, J.D.3
  • 85
    • 0036852241 scopus 로고    scopus 로고
    • Cancer immunoediting: From immunosurveillance to tumor escape
    • DOI 10.1038/ni1102-991
    • Dunn GP, Bruce AT, Ikeda H, et al. Cancer immunoediting: from immunosurveillance to tumor escape. Nature Immunol 2002;3: 991-8. (Pubitemid 35363648)
    • (2002) Nature Immunology , vol.3 , Issue.11 , pp. 991-998
    • Dunn, G.P.1    Bruce, A.T.2    Ikeda, H.3    Old, L.J.4    Schreiber, R.D.5
  • 86
    • 4143141823 scopus 로고    scopus 로고
    • The immunobiology of cancer immunosurveillance and immunoediting
    • DOI 10.1016/j.immuni.2004.07.017, PII S1074761304002092
    • Dunn GP, Old LJ, Schreiber RD. The immunobiology of cancer immunosurveillance and immunoediting. Immunity 2004;21: 137-48. (Pubitemid 39094044)
    • (2004) Immunity , vol.21 , Issue.2 , pp. 137-148
    • Dunn, G.P.1    Old, L.J.2    Schreiber, R.D.3
  • 87
    • 0345375313 scopus 로고    scopus 로고
    • Naturally occurring B-cell responses to breast cancer
    • DOI 10.1007/s00262-003-0409-4
    • Coronella-Wood JA, Hersh EM. Naturally occurring B-cell responses to breast cancer. Cancer Immunol, Immunotherapy: CII 2003;52:715-38. (Pubitemid 37491701)
    • (2003) Cancer Immunology, Immunotherapy , vol.52 , Issue.12 , pp. 715-738
    • Coronella-Wood, J.A.1    Hersh, E.M.2
  • 88
    • 79955469016 scopus 로고    scopus 로고
    • Clinical relevance of autoantibody detection in lung cancer
    • Solassol J, Maudelonde T, Mange A, et al. Clinical relevance of autoantibody detection in lung cancer. J Thorac Oncol 2011;6: 955-62.
    • (2011) J Thorac Oncol , vol.6 , pp. 955-962
    • Solassol, J.1    Maudelonde, T.2    Mange, A.3
  • 90
    • 0029014010 scopus 로고
    • Serum p53 antibodies as early markers of lung cancer
    • Lubin R, Zalcman G, Bouchet L, et al. Serum p53 antibodies as early markers of lung cancer. Nature Med 1995;1:701-2.
    • (1995) Nature Med , vol.1 , pp. 701-702
    • Lubin, R.1    Zalcman, G.2    Bouchet, L.3
  • 91
    • 84860381828 scopus 로고    scopus 로고
    • A proteomics approach for the identification and cloning of monoclonal antibodies from serum
    • Cheung WC, Beausoleil SA, Zhang X, et al. A proteomics approach for the identification and cloning of monoclonal antibodies from serum. Nat Biotechnol 2012;30:447-52.
    • (2012) Nat Biotechnol , vol.30 , pp. 447-452
    • Cheung, W.C.1    Beausoleil, S.A.2    Zhang, X.3
  • 92
    • 57749083520 scopus 로고    scopus 로고
    • Evidence for a human-specific mechanism for diet and antibody-mediated inflammation in carcinoma progression
    • Hedlund M, Padler-Karavani V, Varki NM, et al. Evidence for a human-specific mechanism for diet and antibody-mediated inflammation in carcinoma progression. Proc Natl Acad Sci USA 2008;105:18936-41.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 18936-18941
    • Hedlund, M.1    Padler-Karavani, V.2    Varki, N.M.3
  • 93
    • 79955488798 scopus 로고    scopus 로고
    • Human xeno-autoantibodies against a non-human sialic acid serve as novel serum biomarkers and immunotherapeutics in cancer
    • Padler-Karavani V, Hurtado-Ziola N, Pu M, et al. Human xeno-autoantibodies against a non-human sialic acid serve as novel serum biomarkers and immunotherapeutics in cancer. Cancer Res 2011;71:3352-63.
    • (2011) Cancer Res , vol.71 , pp. 3352-3363
    • Padler-Karavani, V.1    Hurtado-Ziola, N.2    Pu, M.3
  • 94
    • 84863344855 scopus 로고    scopus 로고
    • LC-MS analysis of polyclonal human anti-Neu5Gc xeno-autoantibodies immuno-globulin G Subclass and partial sequence using multistep intravenous immunoglobulin affinity purification and multienzymatic digestion
    • Lu Q, Padler-Karavani V, Yu H, et al. LC-MS analysis of polyclonal human anti-Neu5Gc xeno-autoantibodies immuno-globulin G Subclass and partial sequence using multistep intravenous immunoglobulin affinity purification and multienzymatic digestion. Anal Chem 2012;84:2761-8.
    • (2012) Anal Chem , vol.84 , pp. 2761-2768
    • Lu, Q.1    Padler-Karavani, V.2    Yu, H.3
  • 95
    • 84855951084 scopus 로고    scopus 로고
    • Mass spectrometry analyses of kappa and lambda fractions result in increased number of complementarity-determining region identifications
    • Broodman I, de Costa D, Stingl C, et al. Mass spectrometry analyses of kappa and lambda fractions result in increased number of complementarity- determining region identifications. Proteomics 2012;12:183-91.
    • (2012) Proteomics , vol.12 , pp. 183-191
    • Broodman, I.1    De Costa, D.2    Stingl, C.3
  • 97
    • 84861193566 scopus 로고    scopus 로고
    • Mass spectrometric detection of antigen-specific immunoglobulin peptides in para-neoplastic patient sera
    • Maat P, VanDuijn M, Brouwer E, et al. Mass spectrometric detection of antigen-specific immunoglobulin peptides in para-neoplastic patient sera. J Autoimmun 2012;38:354-60.
    • (2012) J Autoimmun , vol.38 , pp. 354-360
    • Maat, P.1    Vanduijn, M.2    Brouwer, E.3
  • 98
    • 77950998562 scopus 로고    scopus 로고
    • Role of complement in innate immunity and infections
    • Daha MR. Role of complement in innate immunity and infections. Crit Rev Immunol 2010;30:47-52.
    • (2010) Crit Rev Immunol , vol.30 , pp. 47-52
    • Daha, M.R.1
  • 99
    • 77958551232 scopus 로고    scopus 로고
    • Decreased levels of bisecting GlcNAc glycoforms of IgG are associated with human longevity
    • Ruhaak LR, Uh HW, Beekman M, et al. Decreased levels of bisecting GlcNAc glycoforms of IgG are associated with human longevity. PloS one 2010;5:e12566.
    • (2010) PloS One , vol.5
    • Ruhaak, L.R.1    Uh, H.W.2    Beekman, M.3
  • 100
    • 77955354778 scopus 로고    scopus 로고
    • Aberrant IgG galactosylation precedes disease onset, correlates with disease activity, and is prevalent in autoantibodies in rheumatoid arthritis
    • Ercan A, Cui J, Chatterton DE, et al. Aberrant IgG galactosylation precedes disease onset, correlates with disease activity, and is prevalent in autoantibodies in rheumatoid arthritis. Arthrit Rheumat 2010;62:2239-48.
    • (2010) Arthrit Rheumat , vol.62 , pp. 2239-2248
    • Ercan, A.1    Cui, J.2    Chatterton, D.E.3
  • 101
    • 0034130028 scopus 로고    scopus 로고
    • Immunoglobulin G glycosylation and clinical outcome in rheumatoid arthritis during pregnancy
    • Alavi A, Arden N, Spector TD, et al. Immunoglobulin G glycosylation and clinical outcome in rheumatoid arthritis during pregnancy. J Rheumatol 2000;27:1379-85. (Pubitemid 30354031)
    • (2000) Journal of Rheumatology , vol.27 , Issue.6 , pp. 1379-1385
    • Alavi, A.1    Arden, N.2    Spector, T.D.3    Axford, J.S.4
  • 102
    • 0036379420 scopus 로고    scopus 로고
    • Hypogalactosylation of serum IgG in patients with ANCA-associated systemic vasculitis
    • Holland M, Takada K, Okumoto T, et al. Hypogalactosylation of serum IgG in patients with ANCA-associated systemic vasculitis. Clin Exp Immunol 2002;129:183-90.
    • (2002) Clin Exp Immunol , vol.129 , pp. 183-190
    • Holland, M.1    Takada, K.2    Okumoto, T.3
  • 103
    • 61849098877 scopus 로고    scopus 로고
    • Regulated glycosylation patterns of IgG during alloimmune responses against human platelet antigens
    • Wuhrer M, Porcelijn L, Kapur R, et al. Regulated glycosylation patterns of IgG during alloimmune responses against human platelet antigens. J Proteome Res 2009;8:450-6.
    • (2009) J Proteome Res , vol.8 , pp. 450-456
    • Wuhrer, M.1    Porcelijn, L.2    Kapur, R.3
  • 104
    • 77954680167 scopus 로고    scopus 로고
    • The IgG-specific endoglycosidase EndoS inhibits both cellular and complement-mediated autoimmune hemolysis
    • Allhorn M, Briceno JG, Baudino L, et al. The IgG-specific endoglycosidase EndoS inhibits both cellular and complement-mediated autoimmune hemolysis. Blood 2010;115:5080-8.
    • (2010) Blood , vol.115 , pp. 5080-5088
    • Allhorn, M.1    Briceno, J.G.2    Baudino, L.3
  • 105
    • 64549099901 scopus 로고    scopus 로고
    • N-linked glycosyla-tion is an important parameter for optimal selection of cell lines producing biopharmaceutical human IgG
    • van Berkel PH, Gerritsen J, Perdok G, et al. N-linked glycosyla-tion is an important parameter for optimal selection of cell lines producing biopharmaceutical human IgG. Biotechnol Progr 2009; 25:244-51.
    • (2009) Biotechnol Progr , vol.25 , pp. 244-251
    • Van Berkel, P.H.1    Gerritsen, J.2    Perdok, G.3
  • 106
    • 79959973076 scopus 로고    scopus 로고
    • Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes
    • Perdivara I, Peddada SD, Miller FW, et al. Mass spectrometric determination of IgG subclass-specific glycosylation profiles in siblings discordant for myositis syndromes. J Proteome Res 2011; 10:2969-78.
    • (2011) J Proteome Res , vol.10 , pp. 2969-2978
    • Perdivara, I.1    Peddada, S.D.2    Miller, F.W.3
  • 107
    • 79953877355 scopus 로고    scopus 로고
    • IgG fc N-glycosylation changes in Lambert-Eaton myasthenic syndrome and myasthenia gravis
    • Selman MH, Niks EH, Titulaer MJ, et al. IgG fc N-glycosylation changes in Lambert-Eaton myasthenic syndrome and myasthenia gravis. J Proteome Res 2011;10:143-52.
    • (2011) J Proteome Res , vol.10 , pp. 143-152
    • Selman, M.H.1    Niks, E.H.2    Titulaer, M.J.3
  • 109
    • 77249145900 scopus 로고    scopus 로고
    • Evaluation of the specific structures of IgA1 hinge glycopeptide in 30 IgA nephropathy patients by mass spectrometry
    • Odani H, Yamamoto K, Iwayama S, et al. Evaluation of the specific structures of IgA1 hinge glycopeptide in 30 IgA nephropathy patients by mass spectrometry. J Nephrol 2010;23: 70-6.
    • (2010) J Nephrol , vol.23 , pp. 70-76
    • Odani, H.1    Yamamoto, K.2    Iwayama, S.3
  • 110
    • 79956063152 scopus 로고    scopus 로고
    • Laboratory testing for cryoglobulins
    • Motyckova G, Murali M. Laboratory testing for cryoglobulins. Am J Hematol 2011;86:500-2.
    • (2011) Am J Hematol , vol.86 , pp. 500-502
    • Motyckova, G.1    Murali, M.2
  • 111
    • 0041859598 scopus 로고    scopus 로고
    • High resolution proteome analysis of cryoglobulins using Fourier transform-ion cyclotron resonance mass spectrometry
    • DOI 10.1002/pmic.200300482
    • Damoc E, Youhnovski N, Crettaz D, et al. High resolution proteome analysis of cryoglobulins using Fourier transform-ion cyclotron resonance mass spectrometry. Proteomics 2003;3: 1425-33. (Pubitemid 37048067)
    • (2003) Proteomics , vol.3 , Issue.8 , pp. 1425-1433
    • Damoc, E.1    Youhnovski, N.2    Crettaz, D.3    Tissot, J.-D.4    Przybylski, M.5
  • 112
    • 79957673692 scopus 로고    scopus 로고
    • Immune complexome analysis of serum and its application in screening for immune complex antigens in rheumatoid arthritis
    • Ohyama K, Ueki Y, Kawakami A, et al. Immune complexome analysis of serum and its application in screening for immune complex antigens in rheumatoid arthritis. Clin Chem 2011;57: 905-9.
    • (2011) Clin Chem , vol.57 , pp. 905-909
    • Ohyama, K.1    Ueki, Y.2    Kawakami, A.3
  • 113
    • 73949091104 scopus 로고    scopus 로고
    • Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens
    • Vrana JA, Gamez JD, Madden BJ, et al. Classification of amyloidosis by laser microdissection and mass spectrometry-based proteomic analysis in clinical biopsy specimens. Blood 2009;114:4957-9.
    • (2009) Blood , vol.114 , pp. 4957-4959
    • Vrana, J.A.1    Gamez, J.D.2    Madden, B.J.3
  • 114
    • 2342653503 scopus 로고    scopus 로고
    • Characterization of amyloidogenic immunoglobulin light chains directly from serum by on-line immunoaffinity isolation
    • DOI 10.1002/bmc.323
    • Bergen HR, Abraham RS, Johnson KL, et al. Characterization of amyloidogenic immunoglobulin light chains directly from serum by on-line immunoaffinity isolation. Biomed Chromatogr BMC 2004;18:191-201. (Pubitemid 38584838)
    • (2004) Biomedical Chromatography , vol.18 , Issue.3 , pp. 191-201
    • Bergen III, H.R.1    Abraham, R.S.2    Johnson, K.L.3    Bradwell, A.R.4    Naylor, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.